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1geg

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[[Image:1geg.jpg|left|200px]]
[[Image:1geg.jpg|left|200px]]
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{{Structure
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|PDB= 1geg |SIZE=350|CAPTION= <scene name='initialview01'>1geg</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1geg", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetoin_dehydrogenase Acetoin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.5 1.1.1.5] </span>
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|DOMAIN=
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{{STRUCTURE_1geg| PDB=1geg | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1geg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geg OCA], [http://www.ebi.ac.uk/pdbsum/1geg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1geg RCSB]</span>
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'''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE'''
'''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE'''
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[[Category: Otagiri, M.]]
[[Category: Otagiri, M.]]
[[Category: Ui, S.]]
[[Category: Ui, S.]]
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[[Category: sdr family]]
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[[Category: Sdr family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:28:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:42:21 2008''
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Revision as of 14:28, 2 May 2008

Image:1geg.jpg

Template:STRUCTURE 1geg

CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE


Overview

The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 A resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, Gln140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.

About this Structure

1GEG is a Single protein structure of sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA.

Reference

Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms., Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M, J Biochem. 2001 Feb;129(2):205-8. PMID:11173520 Page seeded by OCA on Fri May 2 17:28:19 2008

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